Evidence map›Paper›PMID 33185191›Full record

ArticleeLife2020

Intracellular complexities of acquiring a new enzymatic function revealed by mass-randomisation of active-site residues.

Kelsi R Hall, Katherine J Robins, Elsie M Williams, Michelle H Rich, Mark J Calcott, Janine N Copp, Rory F Little, Ralf Schwörer, Gary B Evans, Wayne M Patrick and 1 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 36% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Mitophagy in relation to chronic inflammation/ROS in aging.Molecular and cellular biochemistry · 2025
    Review
  5. The Catalysis Mechanism ofInternational journal of molecular sciences · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 1 institution in 1 country.

Kelsi R HallSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.
Katherine J RobinsSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.ORCID 0000-0001-5049-4246
Elsie M WilliamsSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.
Michelle H RichSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.ORCID 0000-0003-4876-4029
Mark J CalcottSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.ORCID 0000-0002-7736-8095
Janine N CoppSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.ORCID 0000-0001-6690-0480
Rory F LittleSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.
Ralf SchwörerCentre for Biodiscovery, Victoria University of Wellington, Wellington, New Zealand.ORCID 0000-0002-9352-6559
Gary B EvansCentre for Biodiscovery, Victoria University of Wellington, Wellington, New Zealand.
Wayne M PatrickSchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.ORCID 0000-0002-2718-8053
David F AckerleySchool of Biological Sciences, Victoria University of Wellington, Wellington, Wellington, New Zealand.ORCID 0000-0002-6188-9902
Victoria University of Wellington · NZ

Funding

Cancer Society of New Zealand 18.05Royal Society of New Zealand 15-VUW-037Royal Society of New Zealand 19-VUW-076
6 · The paper itself

Abstract

Selection for a promiscuous enzyme activity provides substantial opportunity for competition between endogenous and newly-encountered substrates to influence the evolutionary trajectory, an aspect that is often overlooked in laboratory directed evolution studies. We selected the

Indexed as

Catalytic DomainChloramphenicolEscherichia coliEscherichia coli ProteinsEvolution, MolecularInactivation, MetabolicMutationNitroreductasesProtein ConformationStructure-Activity RelationshipSubstrate SpecificityChloramphenicolEscherichia coli ProteinsNfsA protein, E coliNitroreductasesbiochemistrychemical biologydirected evolutionE. colienzyme evolutionenzyme promiscuityevolutionary biologynitroreductasesubstrate competition

Identifiers

PMID33185191
PMCPMC7738182
OpenAlexW3100965451

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.